Factors Governing the Mechanism and Efficiency of Porphyrin-Sensitized Photooxidations in Homogeneous Solutions and Organized Media

  • Giulio Jori
  • Elena Reddi
  • Luigi Tomio
  • Fulvio Calzavara
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 160)


Porphyrin-sensitized photoreactions in biological systems usually involve the lowest excited triplet state of the dye [3P] as the reactive intermediate (Spikes, 1975). For most porphyrins [3P] is formed with quantum yield higher than 0.8 (Bonnett et al., 1980). It is generally assumed that in aerated media [3P] is efficiently quenched by oxygen with generation of 1O2 via electronic energy transfer: typical quantum yields for 1O2 production range between 0.40 for tetraphenylporphines (Maillard et al, 1980) and 0.75 for HPD (Dougherty et al., 1976). However, there is increasing evidence that the interaction of [3P] with oxygen (type II mechanism) can originate reactive species other than 1O2, including 1O2, OH, and H2O2 both in homogeneous solutions and in cell systems; [3P] may also undergo e- transfer to or from suitable substrates [S] initiating radical processes (type I mechanism). Selected examples of porphyrin-promoted photoprocesses not involving exclusively 1O2 are shown in Table 1.


Maximal Reaction Rate Free Base Porphyrin Electronic Energy Transfer Thymine Glycol Lower Excited Triplet State 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

cetyl trimethylammonium bromide


3 carbamoyl-2,2,5,5-tetramethylpyrrolidin-l-yloxy


5,5 dimethyl-1-pyrroline-l-oxide






hematoporphyrin derivative


human serum albumin




N-acetyl-L-tryptophan amide


5,10,14,20[4-(N,N’,N’’,-trimethylanil-inium) porphyrin]


sodium dodecylsulphate




meso-tetra-(4-carboxyphenyl)porphine ? TMPH, 2,2,6,6-tetramethylpyridinium chloride




Triton X-100




Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.


  1. 1.
    Almgren, M. and J.K. Thomas (1980) Interfacial electron transfer involving radical ions of carotene and diphenylhexatriene in micelles and vesicles. Photochem. Photobiol. 31, 329–335.CrossRefGoogle Scholar
  2. 2.
    Ballard, S.G. and D.C. Mauzerall (1980) Photochemical ionogenesis in solutions of zinc octaethylporphyrin. J.Chenu Phys. 72, 933–947.CrossRefGoogle Scholar
  3. 3.
    Bonnett, R., A.A. Charalambides and E.J. Land (1980) Triplet states of porphyrin esters. J.C.S. Faraday I, 76, 852–859.CrossRefGoogle Scholar
  4. 4.
    Buettner, G.R. and L.W. Oberley (1979) Superoxide formation by protoporphyrin as seen by spin trapping. FEBS Lett. 98, 18–20.PubMedCrossRefGoogle Scholar
  5. 5.
    Cannistraro, S., G. Jori and A. Van de Vorst (1978a) Photosensitization of amino acids by di-cyan-hemin: kinetic and EPR studies. Photochem. Photobiol. 27, 257–260.CrossRefGoogle Scholar
  6. 6.
    Cannistraro, S., A. Van de Vorst and G. Jori (1981) Quantum yield of electron transfer and of singlet oxygen production by porphyrins: an EPR study. Photobiochem. Photobiophys., in press.Google Scholar
  7. 7.
    Cauzzo, G., G. Gennari, G. Jori and J.D. Spikes (1977) The effect of chemical structure on the photosensitizing efficiency of porphyrins. Photochem. Photobiol. 25, 389–395.PubMedCrossRefGoogle Scholar
  8. 8.
    Cox, G.S., D.G. Whitten and C. Giannotti (1979) Interaction of porphyrin and metalloporphyrin excited states with molecular oxygen. Energy-transfer versus electrontransfer quenching mechanisms in photooxidations. Chem. Phys. Lett. 67, 511–515.CrossRefGoogle Scholar
  9. 9.
    Cozzani, I., G. Jori, E. Reddi, A. Fortunato, L. Tomio and P.L. Zorat (1981). Distribution of endogenous and injected porphyrins at the subcellular level in rat hepatocytes and in ascites hepatoma. Chem.-Biol. Interactions, in press.Google Scholar
  10. 10.
    Dougherty, T.J., C.J. Gomer and K.R. Weishaupt (1976) Energetics and efficiency of photoinactivation of murine tumor cells containing hematoporphyrin. Cancer Res. 36, 2330–2333.PubMedGoogle Scholar
  11. 11.
    Foote, C.S. (1976) “Photosensitized oxidation and singlet oxygen: consequences in biological systems.” In: Free Radicals in Biology (ed., W.A. Pryor), Vol. II, Academic Press, New York, pp.85–133.Google Scholar
  12. 12.
    Genov, N. and G. Jori (1973) Conformational studies on the alkaline protease from Bacillus mesentericus. Int. J. Peptide Protein Res. 5, 127–133.CrossRefGoogle Scholar
  13. 13.
    Girotti, A.W. (1979) Protoporphyrin-sensitized photodamage in isolated membranes of human erythrocytes. Biochem. 18, 4403–4409.CrossRefGoogle Scholar
  14. 14.
    Haining, R.G., E. Hulset and R.F. Labbe (1969) Photo-hemolysis. The comparative behaviour of erythrocytes from patients with different types of porphyria. Proc. Soc. Expl. Biol. Med. 132, 625–628.Google Scholar
  15. 15.
    Hariharan, P.V., J. Courtney and S. Eleczko (1980) Production of hydroxyl radicals in cell systems exposed to hematoporphyrin and red light. Int. J. Radiat. Biol. 37, 691–694.Google Scholar
  16. 16.
    Hopf, F.R. and D.G. Whitten (1975) “Photochemistry of porphyrins and metalloporphyrins” in: Porphyrins and Metalloporphyr ins (ed., K.M. Smith), Elsevier Publishing Co., Amsterdam, pp. 667–700.Google Scholar
  17. 17.
    Horinishi, H., Y. Hachimori, K. Kurihara and K. Shibata (1964) States of amino acid residues in proteins. III. Histidine residues in insulin, lysozyme albumin and proteinases as determined with a new reagent of diazolH-tetrazole. Biochim. Biophys. Acta 86, 477–489.PubMedCrossRefGoogle Scholar
  18. 18.
    Ito, T. (1978) Cellular and subcellular mechanisms of photodynamic action: the singlet oxygen hypothesis as a driving force in recent research. Photochem. Photobiol. 28, 493–508.PubMedCrossRefGoogle Scholar
  19. 19.
    Jori, G., G. Galiazzo and E. Scoffone (1969) Photodynamic action of porphyrins on amino acids and proteins. I. Selective photooxidation of methionine in aqueous solution. Biochem. 8, 2969–2875.Google Scholar
  20. 20.
    Jori G., G. B. Pizzi, E. Reddi, L. Tomio, B. Salvato, P. L. Zorat and F. Calzavara (1979) Time-course of hematoporphyrin distribution in selected tissues and in ascites hepatoma of normal and tumour-bearing rats. Tumori 65, 43–52.Google Scholar
  21. 21.
    Jori G., E. Reddi, E. Rossi, I. Cozzani, L. Tomio, P.L. Zorat, G.B. Pizzi and F. Calzavara (1980) Porphyrin-sensitized photoreactions and their use in cancer phototherapy. Med. Biol. Environ. 8, 139–154.Google Scholar
  22. 22.
    Jori G. and J.D. Spikes (1981) “Photosensitized oxidations in complex biological structures”, In: Oxygen and Oxy-radicals in Chemistry and Biology, (ed., M.A.J. Rodgers and E.L. Powers), Academic Press, New York, pp 441–453.Google Scholar
  23. 23.
    Kessel, D. (1977) Effects of photoactivated porphyrins at the surface of leukemia L1210 cells. Biochem. 16:3443–3449.CrossRefGoogle Scholar
  24. 24.
    Kessel, D. and E. Rossi (1982) Determinants of porphyrin-induced photooxidation characterized by fluorescence and absorption spectra. Photochem. Photobiol., 35, 37–41.CrossRefGoogle Scholar
  25. 25.
    Kohn, K. and D. Kessel (1979) On the mode of cytotoxic action of photoactivated porphyrins. Biochem. Pharmacol. 28, 2465–2470.PubMedCrossRefGoogle Scholar
  26. 26.
    Koskelo P. and U. Muller-Eberhard (1977) Interaction of porphyrins with proteins. Seminars Hematol. 14, 221–226.Google Scholar
  27. 27.
    Lindig B. and M. A. J. Rodgers (1981) Rate parameters for quenching of singlet oxygen by water-soluble and lipid-soluble substrates in aqueous and micellar systems. Photochem. Photobiol. 33, 627–634.CrossRefGoogle Scholar
  28. 28.
    Maillard P., P. Krausz, C. Giannotti and S. Gaspard (1980) Photoinduced activation of molecular oxygen by various porphyrins, bis-porphyrins, phthalocyanines, pyridinoporphyrazines and their metal derivatives. J. Organomet. Chem. 197, 285–290.CrossRefGoogle Scholar
  29. 29.
    Merkel P.B., R. Nilsson and D.R. Kearns (1972) Remarkable solvent effect on the lifetime of singlet oxygen. J. Am. Chem. Soc. 94, 1029–1030.CrossRefGoogle Scholar
  30. 30.
    Reddi E., E. Rossi and G. Jori (1981a) Factors controlling the efficiency of porphyrins as photosensitizers of biological systems to damage by visible light, Med. Biol. Environ. 9, 337–351.Google Scholar
  31. 31.
    Reddi E., F. Ricchelli and G. Jori (1981b) Interaction of human serum albumin with hematoporphyrin and its Zn2+ and Mg2+ derivatives. Int. J. Peptide Prot. Res., in press.Google Scholar
  32. 32.
    Rossi E., A. van de Vorst and G. Jori (1981) Competition between the singlet oxygen and electron transfer mechanisms in the porphyrin-sensitized photooxidation of L-tryptophan and tryptamine in aqueous micellar dispersions. Photochem. Photobiol. 34, 447–454.Google Scholar
  33. 33.
    Sandberg, S. and I. Romslo (1981) Porphyrin-induced photodamage at the cellular and subcellular level as related to the solubility of the porphyrin. Clin. Chim. Acta 109, 193–201.PubMedCrossRefGoogle Scholar
  34. 34.
    Spikes J.D. (1975) Porphyrins and related compounds as photodynamic sensitizers. Ann. N. Y. Acad. Sci. 244, 496–508.PubMedCrossRefGoogle Scholar
  35. 35.
    Tanielian, C. and L. Golder (1981) Quenching of singlet oxygen by sensitizer in dye-sensitized photooxygenation. Photochem. Photobiol. 34, 411–414.Google Scholar
  36. 36.
    Wallace, S.C. and J.K. Thomas (1973) Reactions in micellar systems. Radiat. Res 54, 49–62.PubMedCrossRefGoogle Scholar

Copyright information

© Plenum Press, New York 1983

Authors and Affiliations

  • Giulio Jori
    • 1
  • Elena Reddi
    • 1
  • Luigi Tomio
    • 2
  • Fulvio Calzavara
    • 2
  1. 1.Istituto di Biologia Animale, Centro C.N.R. EmocianineUniversita di PadovaItaly
  2. 2.Divisione di RadioterapiaOspedale Civile di PadovaPadovaItaly

Personalised recommendations